Structural requirements in the transmembrane domain of GLIC revealed by incorporation of noncanonical histidine analogs

Chemistry and Biology

Volumn 21, Issue 12, 2014, Pages 1700-1706

  Rienzo, Matthew ^a   Lummis, Sarah C R ^b   Dougherty, Dennis A ^a  

^a California Institute of Technology   (United States)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYACID; CYANOBACTERIAL PENTAMERIC LIGAND GATED ION CHANNEL GLIC; CYSTEINE LOOP LIGAND GATED ION CHANNEL RECEPTOR; HISTIDINE DERIVATIVE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; HISTIDINE; HYDROXYACID; LIGAND GATED ION CHANNEL;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ELECTROPHYSIOLOGY; HYDROGEN BOND; IN VIVO STUDY; MUTAGENESIS; NONHUMAN; OOCYTE; PROTEIN DOMAIN; PROTEIN STABILITY; SYNTHESIS; XENOPUS LAEVIS; ANALOGS AND DERIVATIVES; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; CYANOBACTERIUM; GENETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

CYANOBACTERIA; EUKARYOTA; XENOPUS LAEVIS;

BACTERIAL PROTEINS; CELL MEMBRANE; CYANOBACTERIA; HISTIDINE; HYDROGEN BONDING; HYDROXY ACIDS; LIGAND-GATED ION CHANNELS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY;

EID: 84919924163     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2014.10.019     Document Type: Article

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